Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin (original) (raw)

Nature volume 292, pages 81–82 (1981)Cite this article

Abstract

Myoglobin (Mb) reversibly binds molecular oxygen in vertebrate muscle and consists of a polypeptide chain of 153 residues and one haem, which closely resembles one subunit of a haemoglobin (Hb) tetramer. In oxygenated myglobin (oxyMb) the iron atom is coordinated by four porphyrin nitrogen atoms, Nε of the invariant ‘proximal’ histidine (F8), and molecular oxygen1. The oxygen molecule lies in a tight pocket, bounded by two hydrophobic groups (Phe CD1 Val E11) and the side chain of the ‘distal’ histidine (E7). This histidine is present in Hb and Mb of many different organisms, with substitution by glutamine or leucine found in only a few cases. The function of the residue is not clear, although it does present steric hindrance to linear ligands such as carbon monoxide and favours ‘bent’ ones, such as O2. We report here that the imidazole stabilizes bound molecular oxygen with a hydrogen bond, as revealed by neutron diffraction analysis.

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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK
    Simon E. V. Phillips
  2. Department of Biology, Brookhaven National Laboratory, Upton, New York, 11973, USA
    Simon E. V. Phillips & Benno P. Schoenborn

Authors

  1. Simon E. V. Phillips
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  2. Benno P. Schoenborn
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Phillips, S., Schoenborn, B. Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin.Nature 292, 81–82 (1981). https://doi.org/10.1038/292081a0

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